Unequivocal estrogen receptor-binding affinity of phthalate esters featured with ring hydroxylation and proper alkyl chain size

Arch Biochem Biophys. 2004 Nov 1;431(1):16-21. doi: 10.1016/j.abb.2004.07.028.

Abstract

The effect of plasticizers phthalate esters (PEs) on health is a controversial subject. PEs are likely to be estrogenic, but the results on the potency obtained by many investigators are still inconsistent and the endocrine disrupting mechanism remains to be clarified. Here, we show that PEs acquire unequivocal binding affinities for human estrogen receptors (ERs) through ring hydroxylation that is possible in the environment and through metabolism. Unexpectedly, the acquired affinities of hydroxylated PEs (PEs-OH) were enhanced by elongation and branching of the ester alkyl chains. PEs-OH with alkyl chains more than six carbons may grope for a new binding site, which is inaccessible to PEs-OH with short chains. The strongest ER-binding affinity among the tested PEs-OH was close to that of diethylstilbestrol, the most potent synthetic ER-binder. Ring hydroxylation would be a new clue to the clarification of the endocrine disruption mechanism of PEs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrocarbons / metabolism*
  • Hydroxylation
  • Phthalic Acids / metabolism*
  • Protein Binding
  • Receptors, Estrogen / metabolism*

Substances

  • Hydrocarbons
  • Phthalic Acids
  • Receptors, Estrogen
  • phthalic acid